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Crystal structure of the computationally designed Pizza2-SR proteinCrystal structure of the computationally designed Pizza2-SR protein
Structural highlights
Publication Abstract from PubMedThe modular structure of many protein families, such as beta-propeller proteins, strongly implies that duplication played an important role in their evolution, leading to highly symmetrical intermediate forms. Previous attempts to create perfectly symmetrical propeller proteins have failed, however. We have therefore developed a new and rapid computational approach to design such proteins. As a test case, we have created a sixfold symmetrical beta-propeller protein and experimentally validated the structure using X-ray crystallography. Each blade consists of 42 residues. Proteins carrying 2-10 identical blades were also expressed and purified. Two or three tandem blades assemble to recreate the highly stable sixfold symmetrical architecture, consistent with the duplication and fusion theory. The other proteins produce different monodisperse complexes, up to 42 blades (180 kDa) in size, which self-assemble according to simple symmetry rules. Our procedure is suitable for creating nano-building blocks from different protein templates of desired symmetry. Computational design of a self-assembling symmetrical beta-propeller protein.,Voet AR, Noguchi H, Addy C, Simoncini D, Terada D, Unzai S, Park SY, Zhang KY, Tame JR Proc Natl Acad Sci U S A. 2014 Oct 21;111(42):15102-7. doi:, 10.1073/pnas.1412768111. Epub 2014 Oct 6. PMID:25288768[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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